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Last update 08 May 2025

BPIFA2

Last update 08 May 2025

Basic Info

Synonyms

bA49G10.1, BPI fold containing family A member 2, BPI fold-containing family A member 2

+ [6]

Introduction

Has strong antibacterial activity against P. aeruginosa.

Drugs associated with BPIFA2

HG-1328

Target

BPIFA2

Mechanism

BPIFA2 modulators

Active Org.-

Originator Org.

Human Genome Sciences, Inc.

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with BPIFA2

100 Translational Medicine associated with BPIFA2

0 Patents (Medical) associated with BPIFA2

Literatures (Medical) associated with BPIFA2

01 Jul 2024·Heliyon

TGF-β1 maintains the developmental potential of embryonic submandibular gland epithelia separated with mesenchyme

Article

Author: Li, Honglin ; Liu, Huabing ; Liu, Liu ; Li, Chunjie ; Cao, Yubin ; Zhao, Guile ; Wang, Guanru

ObjectiveThe objective of this study was to investigate the impact of transforming growth factor β1 (TGF-β1) on epithelial development using an ex vivo model of submandibular gland (SMG) epithelial-mesenchymal separation.Materials and methodsThe ex vivo model was established by separating E13 mouse SMG epithelia and mesenchyme, culturing them independently for 24 h, recombining them, and observing branching morphogenesis. Microarray analysis was performed to evaluate the transcriptome of epithelia treated with and without 1 ng/ml TGF-β1. Differential gene expression, pathway enrichment, and protein-protein interaction networks were analyzed. Quantitative real-time polymerase chain reaction, Western blot, and immunofluorescence were employed to validate the mRNA and protein levels.ResultsRecombined SMGs using separated epithelia and mesenchyme that were cultured for 24 h showed a significant inhibition of epithelial development compared to SMGs recombined immediately after separation. The level of TGF-β1 decreased in the SMG epithelia after epithelia-mesenchyme separation. Epithelia that were separated from mesenchyme for 24 h and pretreated with 1 ng/ml TGF-β1 continued to develop after recombination with mesenchyme, while epithelia without 1 ng/ml TGF-β1 treatment did not. Microarray analysis suggested pathway enrichment related to epithelial development and an upregulation of Sox2 in the 1 ng/ml TGF-β1-treated epithelia. Further experiments validated the phosphorylation of SMAD2 and SMAD3, upregulation of SOX2 and genes associated with epithelial development, including Prol1, Dcpp1, Bhlha15, Smgc, and Bpifa2. Additionally, 1 ng/ml TGF-β1 inhibited epithelial apoptosis by improving the BCL2/BAX ratio and reducing cleaved caspase 3.ConclusionsThe addition of 1 ng/ml TGF-β1 maintained the developmental potential of embryonic SMG epithelia separated from mesenchyme for 24 h. This suggests that 1 ng/ml TGF-β1 may partially compensate for the role of mesenchyme during the separation phase, although its compensation is limited in extent.

01 Feb 2024·Journal of Anatomy

Tlx1 regulates acinar and duct development in mouse salivary glands

Article

Author: Dressler, Keith A. ; Abramson, Cailyn X. G. ; Hand, Arthur R.

AbstractTlx1 encodes a transcription factor expressed in several craniofacial structures of developing mice. The role of Tlx1 in salivary gland development was examined using morphological and immunohistochemical analyses of Tlx1 null mice. Tlx1 is expressed in submandibular and sublingual glands but not parotid glands of neonatal and adult male and female C57Bl/6J (Tlx1+/+) mice. TLX1 protein was localized to the nuclei of terminal tubule cells, developing duct cells and mesenchymal cells in neonatal submandibular and sublingual glands, and to nuclei of duct cells and connective tissue cells in adult glands. Occasionally, TLX1 was observed in nuclei of epithelial cells in or adjacent to the acini. Submandibular glands were smaller and sublingual glands were larger in size in mutant mice (Tlx1−/−) compared to wild‐type mice. Differentiation of terminal tubule and proacinar cells of neonatal Tlx1−/− submandibular glands was abnormal; expression of their characteristic products, submandibular gland protein C and parotid secretory protein, respectively, was reduced. At 3 weeks postnatally, terminal tubule cells at the acinar‐intercalated duct junction were poorly developed or absent in Tlx1−/− mice. Granular convoluted ducts in adult mutant mice were decreased, and epidermal growth factor and nerve growth factor expression were reduced. Along with normal acinar cell proteins, adult acinar cells of Tlx1−/− mice continued to express neonatal proteins and expressed parotid proteins not normally present in submandibular glands. Sublingual gland mucous acinar and serous demilune cell differentiation were altered. Tlx1 is necessary for proper differentiation of submandibular and sublingual gland acinar cells, and granular convoluted ducts. The mechanism(s) underlying Tlx1 regulation of salivary gland development and differentiation remains unknown.

01 May 2022·Oral DiseasesQ3 · MEDICINE

Salivary BPIFA proteins are altered in patients undergoing hematopoietic cell transplantation

Q3 · MEDICINE

Article

Author: Vargas, Pablo Agustin ; Corrêa, Maria Elvira Pizzigatti ; Coletta, Ricardo D. ; Silva, Andreia Aparecida ; Carvalho, Marco Antonio ; Lopes, Márcio Ajudarte ; Bingle, Lynne ; Innocentini, Lara Maria Alencar Ramos ; Bingle, Colin D.

AbstractObjectiveThe aim of this study was to evaluate the expression of BPIFA proteins in the saliva and salivary glands of hematopoietic cell transplant (HCT) patients.Material and MethodsThis longitudinal study included patients who had undergone autologous HCT (auto‐HCT) and allogeneic HCT (allo‐HCT), and unstimulated saliva was collected at three time points, with a fourth collection at oral chronic graft‐versus‐host disease (cGVHD) onset. BPIFA expression was analysed by Western blotting in saliva and immunostaining in the minor salivary glands of cGVHD patients.ResultsAuto‐HCT patients showed increased levels of BPIFA1 (p = .021) and BPIFA2 at D+7 (p = .040), whereas allo‐HCT group demonstrated decreased expression of BPIFA2 at D+8 (p = .002) and at D+80 (p = .001) and a significant association between BPIFA2 low levels and hyposalivation was observed (p = .02). BPIFA2 was significantly lower in the cGVHD patients when compared to baseline (p = .04).ConclusionsThe results of this study show distinct pattern of expression of BPIF proteins in both auto‐HCT and allo‐HCT recipients with decreased levels of BPIFA2 during hyposalivation and cGVHD. Further studies are necessary to elucidate these proteins mechanisms and their clinical implications in these groups of patients.

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BPIFA2

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